Methylation of lysine residues of core histones plays a critical role in the regulation of gene expression.1 Jumonji domain containing 2A (JMJD2A) is the first reported trimethyllysine-specific histone demethylase.2 It catalyzes the demethylation of trimethylated histone at lysine residues 9 and 36.3 Like other JmjC protein hydroxylase family members, JMJD2A is an -ketoglutarate-dependent Fe (II) oxygenase.3 JMJD2As transcriptional function appEArs to depend on protein associations, as it is implicated in both transcriptional silencing and upregulation of the androgen receptor-dependent genes.2 Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylases may be drug discovery targets for therapeutic intervention.1Technical InformationSynonymsJHDM3AJumonji Domain Containing 2AKDM4APurity95% estimated by SDS-PAGESourceRecombinant N-terminal His-tagged protein expressed in E. coliMW43 kDaFormulationA solution in 50 mM Hepes, pH 7.4, containing 150 mM sodium chloride and 20% glycerolUniProt Accession O75164